KCTD6 (3p14.3), KCASH3 , (luonnollinen HDAC inhibiittori KCASH)

https://www.ncbi.nlm.nih.gov/gene/200845

1. NM_001128214.2 → NP_001121686.1  BTB/POZ domain-containing protein KCTD6
   See identical proteins and their annotated locations for NP_001121686.1
   
   

   Conserved Domains (1) summary

   cd18394
   Location:10 → 113

   BTB_POZ_KCTD6; BTB (Broad-Complex, Tramtrack and Bric a brac)/POZ (poxvirus and zinc finger) domain found in potassium channel tetramerization domain-containing protein 6 (KCTD6)

Related articles in PubMed
 

1. Thermal and chemical stability of two homologous POZ/BTB domains of KCTD proteins characterized by a different oligomeric organization. Pirone L, et al. Biomed Res Int, 2013. PMID 24307990, Free PMC Article
2. Cullin 3 Recognition Is Not a Universal Property among KCTD Proteins. Smaldone G, et al. PLoS One, 2015. PMID 25974686, Free PMC Article Cullin 3 (Cul3) recognition by BTB domains is a key process in protein ubiquitination. Among Cul3 binders, a great attention is currently devoted to KCTD proteins, which are implicated in fundamental biological processes. On the basis of the high similarity of BTB domains of these proteins, it has been suggested that the ability to bind Cul3 could be a general property among all KCTDs. In order to gain new insights into KCTD functionality, we here evaluated and/or quantified the binding of Cul3 to the BTB of KCTD proteins, which are known to be involved either in cullin-independent (KCTD12 and KCTD15) or in cullin-mediated (KCTD6 and KCTD11) activities. Our data indicate that KCTD6(BTB) and KCTD11(BTB) bind Cul3 with high affinity forming stable complexes with 4:4 stoichiometries. Conversely, KCTD12(BTB) and KCTD15(BTB) do not interact with Cul3, despite the high level of sequence identity with the BTB domains of cullin binding KCTDs. Intriguingly, comparative sequence analyses indicate that the capability of KCTD proteins to recognize Cul3 has been lost more than once in distinct events along the evolution. Present findings also provide interesting clues on the structural determinants of Cul3-KCTD recognition. Indeed, the characterization of a chimeric variant of KCTD11 demonstrates that the swapping of α2β3 loop between KCTD11(BTB) and KCTD12(BTB) is sufficient to abolish the ability of KCTD11(BTB) to bind Cul3. Finally, present findings, along with previous literature data, provide a virtually complete coverage of Cul3 binding ability of the members of the entire KCTD family.
3. Identification and characterization of KCASH2 and KCASH3, 2 novel Cullin3 adaptors suppressing histone deacetylase and Hedgehog activity in medulloblastoma. De Smaele E, et al. Neoplasia, 2011 Apr. PMID 21472142, Free PMC Article
4. Structural Insights into KCTD Protein Assembly and Cullin3 Recognition. Ji AX, et al. J Mol Biol, 2016 Jan 16. PMID 26334369
5. Obscurin and KCTD6 regulate cullin-dependent small ankyrin-1 (sAnk1.5) protein turnover. Lange S, et al. Mol Biol Cell, 2012 Jul. PMID 22573887, Free PMC Article

See all (24) citations in PubMed

See citations in PubMed for homologs of this gene provided by HomoloGene

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

1. A biophysical characterization of the POZ/BTB of KCTD6, is reported.
2. Obscurin and KCTD6 regulate cullin-dependent small ankyrin-1 (sAnk1.5) protein turnover
3. Rescuing KCASHs expression reduces the Hedgehog-dependent medulloblastoma growth, suggesting that loss of members of this novel family of native HDAC inhibitors is crucial in sustaining Hh pathway-mediated tumorigenesis.